Purification and some properties of elastase from the pancreas of catfish.
- 1 January 1982
- journal article
- Published by Japanese Society of Fisheries Science in NIPPON SUISAN GAKKAISHI
- Vol. 48 (4) , 573-579
- https://doi.org/10.2331/suisan.48.573
Abstract
No elastase activity was detected in the extract of the pancreas of the catfish Paracilurusasotus. However, some activity was found in the extract activated by bovine trypsin or autocatalytically. These facts indicate that elastase is stored as zymogen in the pancreas of the catfish. Two major elastases were found in the autoactivated preparation of the extract of the pancreas. One of the enzymes, designated as elastase B, was purified by CM-cellulose chromatography. The homogeneity of the purified enzyme was demonstrated by polyacrylamide gel electrophoresis in the absence or presence of sodium dodecyl sulfate. Elastase B had strong elastolytic activity as well as Suc-(Ala)8-NA-hydrolyzing activity. The optimum pH and temperature of the enzyme were found to be near pH 8.0 and 50 to 60°C, respectively. Elastase B was found to be stable between pH 5 and 9 below 60°C.Keywords
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